ID   Q6S361_ECOLX            Unreviewed;       265 AA.
AC   Q6S361;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   SubName: Full=Periplasmic chaperone {ECO:0000313|EMBL:AAR85479.1};
DE   Flags: Precursor;
GN   Name=draB {ECO:0000313|EMBL:AAR85479.1};
OS   Escherichia coli.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562 {ECO:0000313|EMBL:AAR85479.1};
RN   [1] {ECO:0000313|EMBL:AAR85479.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IH11128 {ECO:0000313|EMBL:AAR85479.1};
RX   PubMed=15618148; DOI=10.1128/IAI.73.1.135-145.2005;
RA   Piatek R., Zalewska B., Kolaj O., Ferens M., Nowicki B., Kur J.;
RT   "Molecular aspects of biogenesis of Escherichia coli Dr Fimbriae:
RT   characterization of DraB-DraE complexes.";
RL   Infect. Immun. 73:135-145(2005).
RN   [2] {ECO:0007829|PDB:4DJM}
RP   X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) OF 30-265, AND DISULFIDE BONDS.
RA   Dauter Z., Piatek R., Dauter M., Brzuszkiewicz A.;
RT   "Crystal structure of the uropathogenic Escherichia coli chaperone DraB.";
RL   Submitted (FEB-2012) to the PDB data bank.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418,
CC       ECO:0000256|RuleBase:RU003918}.
CC   -!- SIMILARITY: Belongs to the periplasmic pilus chaperone family.
CC       {ECO:0000256|ARBA:ARBA00007399, ECO:0000256|RuleBase:RU003918}.
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DR   EMBL; AY481577; AAR85479.1; -; Genomic_DNA.
DR   RefSeq; WP_021517431.1; NZ_UGBE01000001.1.
DR   PDB; 4DJM; X-ray; 2.52 A; A/B/C/D/E/F/G/H=30-239.
DR   PDBsum; 4DJM; -.
DR   AlphaFoldDB; Q6S361; -.
DR   SMR; Q6S361; -.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IEA:InterPro.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR008962; PapD-like_sf.
DR   InterPro; IPR036316; Pili_assmbl_chap_C_dom_sf.
DR   InterPro; IPR001829; Pili_assmbl_chaperone_bac.
DR   InterPro; IPR016148; Pili_assmbl_chaperone_C.
DR   InterPro; IPR018046; Pili_assmbl_chaperone_CS.
DR   InterPro; IPR016147; Pili_assmbl_chaperone_N.
DR   PANTHER; PTHR30251:SF9; CHAPERONE PROTEIN CAF1M; 1.
DR   PANTHER; PTHR30251; PILUS ASSEMBLY CHAPERONE; 1.
DR   Pfam; PF02753; PapD_C; 1.
DR   Pfam; PF00345; PapD_N; 1.
DR   PRINTS; PR00969; CHAPERONPILI.
DR   SUPFAM; SSF49354; PapD-like; 1.
DR   SUPFAM; SSF49584; Periplasmic chaperone C-domain; 1.
DR   PROSITE; PS00635; PILI_CHAPERONE; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4DJM};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU003918};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..265
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004279521"
FT   DOMAIN          50..178
FT                   /note="Pili assembly chaperone N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00345"
FT   DOMAIN          202..256
FT                   /note="Pili assembly chaperone C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02753"
FT   DISULFID        132..168
FT                   /evidence="ECO:0007829|PDB:4DJM"
SQ   SEQUENCE   265 AA;  28577 MW;  871E0A67FD0F7AE7 CRC64;
     MKMRAVAVFT GMLTGVLSVA GLLSAGAYAA GGEGNMSASA TETNARVFSL HLGATRVVYN
     PASSGETLTV INDQDYPMLV QSEVLSEDQK SPAPFVVTPP LFRLDGQQSS RLRIVRTGGE
     FPPDRESLQW ICVKGIPPKE GDRWAEGKDG EKKADKVSLN VQLSVSSCIK LFVRPPAVKG
     RPDDVAGKVE WQRAGNRLKG VNPTPFYINL STLTVGGKEV KEREYIAPFS SREYPLPAGA
     SGKVQWKVIT DYGGTSKQFE AELKG
//